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High-throughput Screening for Protein-based Inheritance in S. cerevisiae
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Protein inheritance (prions) based on parallel in-register beta-sheet amyloid structures

Reed B Wickner1, Frank Shewmaker, Dmitry Kryndushkin

  • 1Laboratory of Biochemistry and Genetics, National Institute of Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830, USA. wickner@helix.nih.gov

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology
|September 19, 2008
PubMed

Insights

Most prions are self-propagating amyloids found in mammals and fungi. Their structure allows faithful transmission of information, enabling prions to function as genes encoding heritable traits.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Prions are infectious proteins, often existing as self-propagating amyloids (filamentous protein multimers).
  • Prions are observed in diverse species, including mammals and fungi, such as yeast prions [URE3] and [PSI+] and the Podospora anserina prion [Het-s].
  • Some fungal prions, like [Het-s], may have normal cellular functions, contrasting with their pathogenic roles in other contexts.

Purpose of the Study:

  • To elucidate the structural basis of prion propagation and information encoding.
  • To explore the functional parallels between prions and genetic elements.

Main Methods:

  • Structural analysis of prion amyloids.
  • Investigation of self-propagation mechanisms in yeast and fungal models.

Main Results:

  • Prion amyloids possess a parallel in-register beta-sheet structure.
  • This structure facilitates a templating mechanism at filament ends, ensuring faithful transmission of prion variants.
  • The self-reproducing nature of prions allows them to act as non-DNA-based genes, encoding heritable information.

Conclusions:

  • The structural characteristics of prion amyloids are key to their propagation and information transfer.
  • Prions represent a unique class of biological entities that function as heritable genetic elements through protein templating.

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